Factor Xa cleaves SARS-CoV-2 spike protein to block viral entry and infection

[1]  L. Velloso,et al.  Contact and intrinsic coagulation pathways are activated and associated with adverse clinical outcomes in COVID-19 , 2022, Blood Advances.

[2]  S. Rowland-Jones,et al.  Omicron entry route , 2022, Nature Reviews Immunology.

[3]  D. Parums.  Editorial: Current Status of Oral Antiviral Drug Treatments for SARS-CoV-2 Infection in Non-Hospitalized Patients , 2021, Medical science monitor : international medical journal of experimental and clinical research.

[4]  William T. Harvey,et al.  Author Correction: Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies , 2021, Nature.

[5]  Vineet D. Menachery,et al.  The N501Y spike substitution enhances SARS-CoV-2 infection and transmission , 2021, Nature.

[6]  M. Farzan,et al.  Mechanisms of SARS-CoV-2 entry into cells , 2021, Nature reviews. Molecular cell biology.

[7]  J. Tregoning,et al.  Progress of the COVID-19 vaccine effort: viruses, vaccines and variants versus efficacy, effectiveness and escape , 2021, Nature Reviews Immunology.

[8]  J. Tregoning,et al.  Progress of the COVID-19 vaccine effort: viruses, vaccines and variants versus efficacy, effectiveness and escape , 2021, Nature reviews. Immunology.

[9]  P. Sham,et al.  Coagulation factors and the incidence of COVID-19 severity: Mendelian randomization analyses and supporting evidence , 2021, Signal Transduction and Targeted Therapy.

[10]  M. Caligiuri,et al.  The K18-hACE2 Transgenic Mouse Model Recapitulates Non-Severe and Severe COVID-19 in Response to Infectious Dose of SARS-CoV-2 Virus , 2021, bioRxiv.

[11]  M. Giacca,et al.  The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets , 2021, Nature Microbiology.

[12]  W. Ruf.  Roles of factor Xa beyond coagulation , 2021, Journal of Thrombosis and Thrombolysis.

[13]  Jared L. Johnson,et al.  Coagulation factors directly cleave SARS-CoV-2 spike and enhance viral entry , 2021, bioRxiv.

[14]  Graham W. Taylor,et al.  Assessing transmissibility of SARS-CoV-2 lineage B.1.1.7 in England , 2021, Nature.

[15]  N. G. Davies,et al.  Increased mortality in community-tested cases of SARS-CoV-2 lineage B.1.1.7 , 2021, Nature.

[16]  D. Ho,et al.  Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 , 2021, Nature.

[17]  B. Haynes,et al.  SARS-CoV-2 variant B.1.1.7 is susceptible to neutralizing antibodies elicited by ancestral spike vaccines , 2021, Cell Host & Microbe.

[18]  L. Smeeth,et al.  Case fatality risk of the SARS-CoV-2 variant of concern B.1.1.7 in England, 16 November to 5 February , 2021, medRxiv.

[19]  Vineet D. Menachery,et al.  The variant gambit: COVID-19’s next move , 2021, Cell Host & Microbe.

[20]  M. Beer,et al.  SARS-CoV-2 spike D614G change enhances replication and transmission , 2021, Nature.

[21]  Neville E. Sanjana,et al.  The Spike D614G mutation increases SARS-CoV-2 infection of multiple human cell types , 2021, eLife.

[22]  Vineet D. Menachery,et al.  Infection and mRNA-1273 vaccine antibodies neutralize SARS-CoV-2 UK variant , 2021, medRxiv.

[23]  Vineet D. Menachery,et al.  Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis , 2021, Nature.

[24]  S. Knudsen,et al.  Stenoparib, an Inhibitor of Cellular Poly(ADP-Ribose) Polymerase, Blocks Replication of the SARS-CoV-2 and HCoV-NL63 Human Coronaviruses In Vitro , 2021, mBio.

[25]  Lin‐Fa Wang,et al.  Lessons from the host defences of bats, a unique viral reservoir , 2021, Nature.

[26]  Carl A. B. Pearson,et al.  Estimated transmissibility and impact of SARS-CoV-2 lineage B.1.1.7 in England , 2021, Science.

[27]  S. Iliceto,et al.  Reduction in all-cause mortality in COVID-19 patients on chronic oral anticoagulation: A population-based propensity score matched study , 2020, International Journal of Cardiology.

[28]  S. Melino,et al.  New Consensus pattern in Spike CoV-2: potential implications in coagulation process and cell–cell fusion , 2020, Cell death discovery.

[29]  A. Fontanella,et al.  Thromboprofilaxys With Fondaparinux vs. Enoxaparin in Hospitalized COVID-19 Patients: A Multicenter Italian Observational Study , 2020, Frontiers in Medicine.

[30]  Mulin Jun Li,et al.  Coagulation factors and COVID-19 severity: Mendelian randomization analyses and supporting evidence , 2020, medRxiv.

[31]  C. Macaya,et al.  Clinical profile and prognosis in patients on oral anticoagulation before admission for COVID‐19 , 2020, European journal of clinical investigation.

[32]  Zhènglì Shí,et al.  Characteristics of SARS-CoV-2 and COVID-19 , 2020, Nature Reviews Microbiology.

[33]  G. Frydman,et al.  The Potential Role of Coagulation Factor Xa in the Pathophysiology of COVID-19: A Role for Anticoagulants as Multimodal Therapeutic Agents , 2020, TH Open.

[34]  R. Al‐Horani.  Potential Therapeutic Roles for Direct Factor Xa Inhibitors in Coronavirus Infections , 2020, American Journal of Cardiovascular Drugs.

[35]  Vineet D. Menachery,et al.  Spike mutation D614G alters SARS-CoV-2 fitness and neutralization susceptibility , 2020, Nature.

[36]  Shuwen Liu,et al.  Structural and functional properties of SARS-CoV-2 spike protein: potential antivirus drug development for COVID-19 , 2020, Acta Pharmacologica Sinica.

[37]  D. A. Stein,et al.  TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells , 2020, Life Science Alliance.

[38]  C. Hallam,et al.  Lethality of SARS-CoV-2 infection in K18 human angiotensin-converting enzyme 2 transgenic mice , 2020, Nature Communications.

[39]  Nan Tang,et al.  Pulmonary alveolar regeneration in adult COVID-19 patients , 2020, Cell Research.

[40]  S. Rowland-Jones,et al.  Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases Infectivity of the COVID-19 Virus , 2020, Cell.

[41]  John A.G. Briggs,et al.  A thermostable, closed SARS-CoV-2 spike protein trimer , 2020, Nature Structural & Molecular Biology.

[42]  M. Diamond,et al.  Growth, detection, quantification, and inactivation of SARS-CoV-2 , 2020, Virology.

[43]  W. Xu,et al.  The role of furin cleavage site in SARS-CoV-2 spike protein-mediated membrane fusion in the presence or absence of trypsin , 2020, Signal Transduction and Targeted Therapy.

[44]  D. Fremont,et al.  Cholesterol 25-hydroxylase suppresses SARS-CoV-2 replication by blocking membrane fusion , 2020, Proceedings of the National Academy of Sciences.

[45]  S. Khurana,et al.  Antibody signature induced by SARS-CoV-2 spike protein immunogens in rabbits , 2020, Science Translational Medicine.

[46]  D. Leaf,et al.  COVID-19 and coagulation: bleeding and thrombotic manifestations of SARS-CoV-2 infection , 2020, Blood.

[47]  A. Geronikaki,et al.  In Silico Evaluation of the Effectivity of Approved Protease Inhibitors against the Main Protease of the Novel SARS-CoV-2 Virus , 2020, Molecules.

[48]  L. Saso,et al.  Targeting host cell proteases to prevent SARS-CoV-2 invasion. , 2020, Current drug targets.

[49]  A. Wells,et al.  Pulmonary fibrosis and COVID-19: the potential role for antifibrotic therapy , 2020, The Lancet Respiratory Medicine.

[50]  M. Hoffmann,et al.  A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells , 2020, Molecular Cell.

[51]  R. José,et al.  COVID-19 cytokine storm: the interplay between inflammation and coagulation , 2020, The Lancet Respiratory Medicine.

[52]  F. Sariali̇oğlu,et al.  The old but new: Can unfractioned heparin and low molecular weight heparins inhibit proteolytic activation and cellular internalization of SARS-CoV2 by inhibition of host cell proteases? , 2020, Medical Hypotheses.

[53]  K. Yuen,et al.  Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2 , 2020, Cell.

[54]  S. Ghasemi,et al.  Genotype and phenotype of COVID-19: Their roles in pathogenesis , 2020, Journal of Microbiology, Immunology and Infection.

[55]  Yan Liu,et al.  Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV , 2020, Nature Communications.

[56]  G. Herrler,et al.  SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor , 2020, Cell.

[57]  L. Poon,et al.  Complete Genome Sequence of a 2019 Novel Coronavirus (SARS-CoV-2) Strain Isolated in Nepal , 2020, Microbiology Resource Announcements.

[58]  P. Hsu,et al.  A Population-Based Propensity Score-Matched Study to Assess the Impact of Repeated Vaccination on Vaccine Effectiveness for Influenza-Associated Hospitalization Among the Elderly , 2020, Clinical interventions in aging.

[59]  W. Xu,et al.  Fusion mechanism of 2019-nCoV and fusion inhibitors targeting HR1 domain in spike protein , 2020, Cellular & Molecular Immunology.

[60]  J. Luban.  SARS-CoV-2 , 2020 .

[61]  A. Goette,et al.  Coagulation factor Xa induces an inflammatory signalling by activation of protease-activated receptors in human atrial tissue. , 2013, European journal of pharmacology.

[62]  P. Conley,et al.  A specific antidote for reversal of anticoagulation by direct and indirect inhibitors of coagulation factor Xa , 2013, Nature Medicine.

[63]  H. Rupprecht,et al.  Clinical Pharmacology of Direct and Indirect Factor Xa Inhibitors , 2010, Drugs.

[64]  A. Bitonti,et al.  Prolonged activity of factor IX as a monomeric Fc fusion protein. , 2010, Blood.

[65]  V. Preedy,et al.  Prospective Cohort Study , 2010 .

[66]  B. Lentz,et al.  Factor XA binding to phosphatidylserine-containing membranes produces an inactive membrane-bound dimer. , 2009, Biophysical journal.

[67]  K. Yuen,et al.  Cleavage of spike protein of SARS coronavirus by protease factor Xa is associated with viral infectivity , 2007, Biochemical and Biophysical Research Communications.

[68]  M. Chiariello,et al.  Involvement of Tissue Factor Pathway Inhibitor in the Coronary Circulation of Patients With Acute Coronary Syndromes , 2003, Circulation.

[69]  Huanming Yang,et al.  Complete Genome Sequences of the SARS-CoV: the BJ Group (Isolates BJ01-BJ04) , 2003, Genomics, Proteomics & Bioinformatics.